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[G-肌动蛋白变性的量热研究]

[Calorimetric study of G-actin denaturation].

作者信息

Tatunashvili L V, Privalov P L

出版信息

Biofizika. 1984 Jul-Aug;29(4):583-5.

PMID:6487667
Abstract

The investigation of G-actin heat denaturation at various pH of the solution by scanning microcalorimetry has shown that unfolding of G-actin is not a two-state process. Since the protein structure does not behave as a single cooperative unit during heat denaturation, it is suggested that the G-actin globule consists, at least, of two interacting domains.

摘要

通过扫描量热法对不同pH值溶液中G-肌动蛋白热变性的研究表明，G-肌动蛋白的去折叠不是一个两态过程。由于蛋白质结构在热变性过程中并非作为一个单一的协同单元起作用，因此有人提出G-肌动蛋白球状体至少由两个相互作用的结构域组成。

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引用本文的文献

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Actinous enigma or enigmatic actin: Folding, structure, and functions of the most abundant eukaryotic protein.肌动蛋白之谜或神秘的肌动蛋白：最丰富的真核生物蛋白质的折叠、结构与功能
Intrinsically Disord Proteins. 2014 Aug 15;2(1):e34500. doi: 10.4161/idp.34500. eCollection 2014.
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Effect of self-association on the structural organization of partially folded proteins: inactivated actin.
自缔合对部分折叠蛋白质结构组织的影响：失活肌动蛋白。
Biophys J. 1999 Nov;77(5):2788-800. doi: 10.1016/S0006-3495(99)77111-0.